Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains.
The substrate-binding domains of six glycanases from Streptomyces lividans were investigated to determine their specificity towards cellulose and xylan. Based upon amino acid sequence similarities, four of the six domains could be assigned to existing cellulose-binding domain families. However, the binding domains of xylanase A and arabinofuranosidase B could not be classified in any of the known families and should therefore be classified as members of a new family. Evidence is also presented that this new family is one of true xylan-binding domains.
Dupont
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Centre de Recherche en Microbiologie Appliquée, Institut Armand-Frappier, Université du Québec, Laval-des-Rapides, C.P. 100, Québec, Canada H7N 4Z3.
Roberge
M
M
Shareck
F
F
Morosoli
R
R
Kluepfel
D
D
D000595:Amino Acid Sequence; D001665:Binding Sites; D002482:Cellulose / Q000378:metabolism; D016384:Consensus Sequence; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012995:Solubility; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D014990:Xylans / Q000378:metabolism*
D014990:Xylans; D002482:Cellulose; D006026:Glycoside Hydrolases; C020668:glycanase